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Investigating Apoptozole as a Chemical Probe for HSP70 Inhibition.

The use of chemical tools to validate clinical targets has gained in popularity over recent years and the importance of understanding the activity, selectivity and mechanism of action of these compounds is well recognized. Dysregulation of the HSP70 protein family has been linked to multiple cancer... Full description

Journal Title: PloS one 2015, Vol.10(10), p.e0140006
Main Author: Evans, Lindsay E
Other Authors: Cheeseman, Matthew D , Yahya, Norhakim , Jones, Keith
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0140006
Link: http://search.proquest.com/docview/1722185543/?pq-origsite=primo
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recordid: proquest1722185543
title: Investigating Apoptozole as a Chemical Probe for HSP70 Inhibition.
format: Article
creator:
  • Evans, Lindsay E
  • Cheeseman, Matthew D
  • Yahya, Norhakim
  • Jones, Keith
subjects:
  • Adenosine Triphosphate–Chemistry
  • Animals–Chemistry
  • Antineoplastic Agents–Metabolism
  • Benzamides–Chemistry
  • Binding Sites–Metabolism
  • Dynamic Light Scattering–Chemistry
  • Fluorescent Dyes–Chemistry
  • Hsc70 Heat-Shock Proteins–Metabolism
  • Hsp70 Heat-Shock Proteins–Chemistry
  • Humans–Metabolism
  • Imidazoles–Chemistry
  • Protein Binding–Metabolism
  • Protein Isoforms–Metabolism
  • Rats–Metabolism
  • Surface Plasmon Resonance–Metabolism
  • Antineoplastic Agents
  • Benzamides
  • Fluorescent Dyes
  • Hsc70 Heat-Shock Proteins
  • Hsp70 Heat-Shock Proteins
  • Imidazoles
  • Protein Isoforms
  • Apoptozole
  • Adenosine Triphosphate
ispartof: PloS one, 2015, Vol.10(10), p.e0140006
description: The use of chemical tools to validate clinical targets has gained in popularity over recent years and the importance of understanding the activity, selectivity and mechanism of action of these compounds is well recognized. Dysregulation of the HSP70 protein family has been linked to multiple cancer types and drug resistance, highlighting their importance as popular targets for anti-cancer drug development. Apoptozole is a recently identified small molecule, which has been reported to possess strong affinity for the HSP70 isoforms HSP72 and HSC70. We investigated apoptozole as a potential chemical tool for HSP70 inhibition. Unfortunately, using both biochemical and biophysical techniques, we were unable to find any experimental evidence that apoptozole binds to HSP70 in a specific and developable way. Instead, we provide experimental evidence that apoptozole forms aggregates under aqueous conditions that could interact with HSP70 proteins in a non-specific manner.
language: eng
source:
identifier: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0140006
fulltext: fulltext
issn:
  • 19326203
  • 1932-6203
url: Link


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titleInvestigating Apoptozole as a Chemical Probe for HSP70 Inhibition.
creatorEvans, Lindsay E ; Cheeseman, Matthew D ; Yahya, Norhakim ; Jones, Keith
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identifierE-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0140006
subjectAdenosine Triphosphate–Chemistry ; Animals–Chemistry ; Antineoplastic Agents–Metabolism ; Benzamides–Chemistry ; Binding Sites–Metabolism ; Dynamic Light Scattering–Chemistry ; Fluorescent Dyes–Chemistry ; Hsc70 Heat-Shock Proteins–Metabolism ; Hsp70 Heat-Shock Proteins–Chemistry ; Humans–Metabolism ; Imidazoles–Chemistry ; Protein Binding–Metabolism ; Protein Isoforms–Metabolism ; Rats–Metabolism ; Surface Plasmon Resonance–Metabolism ; Antineoplastic Agents ; Benzamides ; Fluorescent Dyes ; Hsc70 Heat-Shock Proteins ; Hsp70 Heat-Shock Proteins ; Imidazoles ; Protein Isoforms ; Apoptozole ; Adenosine Triphosphate
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descriptionThe use of chemical tools to validate clinical targets has gained in popularity over recent years and the importance of understanding the activity, selectivity and mechanism of action of these compounds is well recognized. Dysregulation of the HSP70 protein family has been linked to multiple cancer types and drug resistance, highlighting their importance as popular targets for anti-cancer drug development. Apoptozole is a recently identified small molecule, which has been reported to possess strong affinity for the HSP70 isoforms HSP72 and HSC70. We investigated apoptozole as a potential chemical tool for HSP70 inhibition. Unfortunately, using both biochemical and biophysical techniques, we were unable to find any experimental evidence that apoptozole binds to HSP70 in a specific and developable way. Instead, we provide experimental evidence that apoptozole forms aggregates under aqueous conditions that could interact with HSP70 proteins in a non-specific manner.
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